Biological Molecules Flashcards

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1
Q

Define metabolism

A

The sum total of auto biochemical reactions taking place in the cells of an organism

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2
Q

Define monomer

A

Single small molecules

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3
Q

Define polymers

A

Large molecules made of many similar monomers covalent bonded together

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4
Q

What are the key biological molecules?

A

Carbohydrates / proteins / lipids / nucleic acids

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5
Q

Name the polymer and monomer of carbs

A

Polymer - polysaccharides
Monomer - monosaccharides

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6
Q

Name the polymer and monomer of proteins

A

Polymer - polypeptides
Monomer- amino acid

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7
Q

Name a polymer and monomer of nucleic acids

A

Polymer-polynucleotide
Monomer- nucleic acid / nucleotide

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8
Q

what is anabolism?

A

Building up large molecules from smaller ones

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9
Q

What are catabolic reactions?

A

Breaking down large molecules to form small ones

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10
Q

What is a condensation reaction?

A

The chemical reaction that combines biological monomers
A new covalent bond formed with a water molecule released

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11
Q

What is a hydrolysis reaction?

A

Splitting large molecules into smaller ones
A covalent bond’s broken and a water molecule is used

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12
Q

What are carbohydrates used for?

A

ATP production for use in respiration
To be stored as glycogen in the. Liver and muscles

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13
Q

What is the most common type of carbohydrate?
Give its structure and key facts.

A

The most common carbohydrate is glucose
Glucose is a polar molecule meaning it is water soluble
Glucose is a hexose sugar

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14
Q

What is the most common type of carbohydrate?
Give its structure and key facts.

A

The most common carbohydrate is glucose
Glucose is a polar molecule meaning it is water soluble
Glucose is a hexose sugar

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15
Q

What is an isomer?

A

Molecules that have the same chemical formula
Alpha + beta glucose

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16
Q

What is alpha glucose?

A

On alpha glucose the hydroxyl group is on carbon 1
Used for energy storage forming nighty branched polymers - glycogen
Starch + glycogen
Water soluble

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17
Q

What is beta glucose?

A

The hydroxyl group found on carbon 1 is above the ring structure
Forms plane cell walls and cellulose

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18
Q

Draw the condensation reaction between 2 alpha glucose monomers to form the disaccharide maltose

A
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19
Q

What is the bond between 2 carbohydrates called?
What’s the bond between z alpha glucose monomers called?

A

Glycosidic bond
1-4 glycosidic bond

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20
Q

What is starch an example of?

A

Starch is an example of a polysaccharide

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21
Q

What is the structure of starch?

A

Large polysaccharide joined by glycosidic bonds
Insoluble, coiled and compact molecules
Amylose alpha glucose monomers joined by 1-4 glycosidic bonds

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22
Q

What is amylopectin?

A

Is a branched polymer with the 1,4 glycosidic bonds between the alpha glucose and glycosidicbonds former between C1 and C6 adjacent alpha glucose

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23
Q

What is the function of starch?

A

Easily transported and used in respiration when hydrolysed.

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24
Q

what is glycogen?

A

a polysaccharide found in animals and bacteria

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25
Q

what is the structure of starch?

A

large insoluble polysaccharide formed by condensation between alpha glucose with both 1,4 and 1,6 glycosidic bonds
highly branched so that they glycosidic bonds can be rapidlly hydrolysed

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26
Q

what is the fucntion of glycogen?

A

can be easily transported and used in respiration once hydrolysed by enzymes

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27
Q

do polysaccharides affect the potential?

A

they do not as they are highly coiled and isoluble
if they did - the water potential would decrease, water molecules would move into the cell and the cells would burst

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28
Q

what are the uses of proteins?

A

enyzmes / structural functions / hormones - insulin / hormone receptors / antiodies / antigens / transport proteins

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29
Q

what are proteins made from?

A

amino acids

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30
Q

what are 1, 2 and 3?

A

1 - amine group (NH2)
2- variable group (changes per amino acid)
3- carboxyl group (COOH)

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31
Q

how many amic acids are there and how are they joined together?

A

there are 20 naturally occuring amino acids
they are joined together by peptide bonds

32
Q

if the varible group is hydrogen, what is the amino acid formed?

A

glycine

33
Q

what is removed when joining together 2 amino acids?

A

a water molecule is removed as it is a condensation reaction

34
Q

what is the primary structure?

A

the simplest level of protein structure, with a specific number of and sequence of amino acids to make up a polypeptide chain

35
Q

why is the primary structre of a protein so important?

A

the primary structure determins the final proteins function

36
Q

what bonds are present in the primary structure?

A

only peptide bonds are present

37
Q

what is the secondary structure?

A

this is the folding of the primary structure into alpha helices or beta pleated sheets

38
Q

what bonds are present in the secondary structure?

A

peptide bonds between amino acids
hydrogen bonds between oxygen and hydrogen - weak but help maintain shape

39
Q

name and describe structure A?

A

alpha helix
a coiled structure, that is strong due to many hydrogen bonds

40
Q

name and describe structure B?

A

beta pleated sheet
a flat flexible structure consisting of parallel polypeptide chains caused by foldings that are cross-linked by hydrogen bonds

41
Q

what is a tertiary structure?

A

formed when the secondary structure folds into a precise, 3D shape - alpha helices and beta pleated sheets
some globular proteins are complete at this stage (some enzymes)
polypeptides are now proteins

42
Q

what bonds are present in tertiary structures?

A

peptide bond sbetween amino acids
hydrogen bonds between nehatively charged R groups and positive hydrogens
ionic bonds between oppositely charges R groups of amino acids
disulfide bridge between 2 sulfur atoms between 2 R groups on cysteien amino acids

43
Q

name A, B, C and D

A

A - hydrophobic interations and Van der Waals forces
B - hydrogen bond
C - disulfide bridge
D - ionic bond

44
Q

what are hydrophobic interactions?

A

hydrophobic interations are when the hydrophobic R groups fold inwards towards the center of the structure - these help maintain the shape

45
Q

what are Van der Waals forces?

A

wesak interactions, not between structures and particular part

46
Q

what are quaternary structures?

A

proteins that rae made of two or more polypeptide chains and a prosthetic group on occasion

47
Q

define prosthetic group and their function

A

chemic groups bonded to proteins but not made of amino acids
important of the function. of proteins

48
Q

what are the 2 categories of quaternary proteins?

A

globular and fibrous proteins

49
Q

what are globlar proteins?

A

globular proteins tend to be soluble in water and make up enzymes, antibodies and hormones
globular proteins have a wide range of amino acid sequence in their structure

50
Q

what is the typical shape of globular proteins?

A

compact ball like shapes
hydrophobic R-group amino acid turned inwards
hydrophilic R-group amino acids turned outwards

51
Q

what is haemoglobin?

A

haemogloblin is a quaternary structure as it is made up og 4 globular ploypeptide chains
each polypeptide chain has a prosthetic group called haem
haem contains iron which bonds to oxygen

52
Q

what are fibrous proteins?

A

fibrous proteins are insoluble and normally provide a structural function
they have a regular, repetitive amino acid sequence

53
Q

what is the shape of fibrous proteins?

A

long, elongated fibres
rigid/strng due to tightly coled triple helices

54
Q

what is college?

A

collegen is a fibrous protein found in large quantaties in connective tissues throughout the human body

55
Q

Name 2 lipid groups

A

Triglycerides and phospholipids

56
Q

What do lipids contain?

A

Carbon, hydrogen, oxygen
→ the proponion of oxygen is very small compared to carbohydrates

57
Q

Are lipids polymers? Why?

A

Not polymers → not made of repeating units

58
Q

What are triglycerides?

A

One glycerol molecule joined to 3 fatty acids by covalent ester bonds.

59
Q

How many fatty acids are there?

A

70 fatty acids with a COOH group with a carbohydrate chain attached

60
Q

What are the functions of triglyceride?

A

Functions include: source of energy → nigh hydrogen percentage, easily oxidised / acts as insulators → for the body and electrical impulses my lean sheath to nerve cues / large non-polar molecules / insoluble e in water / protection for vital organs.

61
Q

What is a mono - unsaturated triglyceride?

A

A triglyceride with one c= c double bond.

62
Q

What is a poly-unsaturated triglyceride?

A

A triglyceride with more than one c c= C double bond

63
Q

What is a phospholipid?

A

A phospholipid has a molecule of glycerol, only 2 fatty acid tail anda phosphate group

64
Q

What are nucleicacias?

A

Large polymers found in the nucleus of a cell
Deoxyribonucleic acid → no oxygen
Ribonucleic acid → with oxygen

65
Q

Describe the monomer for both nucleic acids

A

Nucleotides:
A pentose sugar → 5 carbon sugar
A phosphate group
A nitrogenous base (organic base)

66
Q

State key information about DNA and draw its structure

A

DNA:
Double helix held together by hydrogen bonds → stable
2 hydrogen bonds between adenine and thymine
3 hydrogen bonds between cytosine and guanine
Long chain
Deoxyribose sugar
Adenine/thymine/cytosine/ guanine

67
Q

State key information about RNA and draw its structure

A

RNA:
Single strand with no hydrogen bonds → unstable
Short chain
Ribose sugar
Adenine/guanine/cytosine/uracil

68
Q

What are polynucleotides?

A

A very strong structure of polymerised nucleotides

69
Q

How are nucleotides bonded?

A

A covalent bonds called a phosphodiester between the phosphate group of one nucleotide and the sugar of the adjacent nucleotide
→ forming a sugar phosphate backbone

70
Q

Describe the structure of DNA

A

Double stranded which run in opposite directions (antiparallel)
Held together by hydrogen bonds

71
Q

What is messenger RNA?

A

A copy of the genetic code required to make a protein
→ The genetic code round on RNA is called a codon

72
Q

Key facts of the structure of mRNA

A

→ single polynucleotide strand (curved but still one strand)
→ clover leaf shape with some base pairings
→ uracil and ribose sugar
→ no set organic base ratio
→ 75 nucleotides long

73
Q

What is transfer RNA?

A

tRNA brings amino acids to the ribosomes in a specific order
→ the genetic code on tRNA found in 3 is called an anticodon

74
Q

Key facts of the structure of tRNA

A

→ single polynucleotide strand
→ linear, no base pairing
→ uracil base and ribose sugar
→ No set organic base ratio
→ varies in length (few thousand nucleotides as a maximum)

75
Q

How many types of t RNA are there?

A

61 types